Transmembrane interaction mediates complex formation between peptidase homologues and Kv4 channels
An asthma-related peptidase homologue (DPP10) may act as an auxiliary subunit of Kv4 channels, similar to DPPX. Here we show that DPP10 preferentially binds to Kv4 channel proteins to increase current density and alter channel gating. DPP10 also forms complexes by themselves and with DPPX in the abs...
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| Veröffentlicht in: | Molecular and cellular neuroscience 2005-06, Vol.29 (2), p.320-332 |
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| creator | Ren, Xiaomeng Hayashi, Yukio Yoshimura, Naoki Takimoto, Koichi |
| description | An asthma-related peptidase homologue (DPP10) may act as an auxiliary subunit of Kv4 channels, similar to DPPX. Here we show that DPP10 preferentially binds to Kv4 channel proteins to increase current density and alter channel gating. DPP10 also forms complexes by themselves and with DPPX in the absence of Kv4 channels. DPP10 mRNA is abundantly expressed in nodose and dorsal root ganglia, suggesting that DPP10 participates in controlling airway reactivity and mechanosensation. The region from the N-terminus to the end of the transmembrane of DPP10 mediates its association with the channel, whereas the S1–S2 portion of the channel is sufficient for complex formation. This N-terminal portion of DPP10 also confers all the gating effects produced by the peptidase homologue. Thus, interaction between transmembranes of DPP10/DPPX and Kv4 channel mediates functional complex formation. We call this protein DPPY, instead of DPP10, because of its revealed role as a Kv4 channel regulator. |
| doi_str_mv | 10.1016/j.mcn.2005.02.003 |
| format | Article |
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Here we show that DPP10 preferentially binds to Kv4 channel proteins to increase current density and alter channel gating. DPP10 also forms complexes by themselves and with DPPX in the absence of Kv4 channels. DPP10 mRNA is abundantly expressed in nodose and dorsal root ganglia, suggesting that DPP10 participates in controlling airway reactivity and mechanosensation. The region from the N-terminus to the end of the transmembrane of DPP10 mediates its association with the channel, whereas the S1–S2 portion of the channel is sufficient for complex formation. This N-terminal portion of DPP10 also confers all the gating effects produced by the peptidase homologue. Thus, interaction between transmembranes of DPP10/DPPX and Kv4 channel mediates functional complex formation. We call this protein DPPY, instead of DPP10, because of its revealed role as a Kv4 channel regulator.</description><identifier>ISSN: 1044-7431</identifier><identifier>EISSN: 1095-9327</identifier><identifier>DOI: 10.1016/j.mcn.2005.02.003</identifier><identifier>PMID: 15911355</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Alternative Splicing - physiology ; Animals ; Cell Membrane - metabolism ; CHO Cells ; Cricetinae ; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - genetics ; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - metabolism ; Ganglia, Spinal - metabolism ; Humans ; Ion Channel Gating - physiology ; Macromolecular Substances - metabolism ; Male ; Molecular Sequence Data ; Nerve Tissue Proteins - genetics ; Nerve Tissue Proteins - metabolism ; Neurons, Afferent - metabolism ; Nodose Ganglion - metabolism ; Potassium Channels - genetics ; Potassium Channels - metabolism ; Potassium Channels, Voltage-Gated - metabolism ; Protein Isoforms - genetics ; Protein Isoforms - metabolism ; Protein Subunits - metabolism ; Rats ; Rats, Sprague-Dawley ; Sequence Homology, Amino Acid ; Shal Potassium Channels</subject><ispartof>Molecular and cellular neuroscience, 2005-06, Vol.29 (2), p.320-332</ispartof><rights>2005 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c479t-35df8296ad87ff8e301f784e8141319b329f2cc1418853b2c93d678de1cd2ff73</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.mcn.2005.02.003$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15911355$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ren, Xiaomeng</creatorcontrib><creatorcontrib>Hayashi, Yukio</creatorcontrib><creatorcontrib>Yoshimura, Naoki</creatorcontrib><creatorcontrib>Takimoto, Koichi</creatorcontrib><title>Transmembrane interaction mediates complex formation between peptidase homologues and Kv4 channels</title><title>Molecular and cellular neuroscience</title><addtitle>Mol Cell Neurosci</addtitle><description>An asthma-related peptidase homologue (DPP10) may act as an auxiliary subunit of Kv4 channels, similar to DPPX. Here we show that DPP10 preferentially binds to Kv4 channel proteins to increase current density and alter channel gating. DPP10 also forms complexes by themselves and with DPPX in the absence of Kv4 channels. DPP10 mRNA is abundantly expressed in nodose and dorsal root ganglia, suggesting that DPP10 participates in controlling airway reactivity and mechanosensation. The region from the N-terminus to the end of the transmembrane of DPP10 mediates its association with the channel, whereas the S1–S2 portion of the channel is sufficient for complex formation. This N-terminal portion of DPP10 also confers all the gating effects produced by the peptidase homologue. Thus, interaction between transmembranes of DPP10/DPPX and Kv4 channel mediates functional complex formation. We call this protein DPPY, instead of DPP10, because of its revealed role as a Kv4 channel regulator.</description><subject>Alternative Splicing - physiology</subject><subject>Animals</subject><subject>Cell Membrane - metabolism</subject><subject>CHO Cells</subject><subject>Cricetinae</subject><subject>Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - genetics</subject><subject>Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - metabolism</subject><subject>Ganglia, Spinal - metabolism</subject><subject>Humans</subject><subject>Ion Channel Gating - physiology</subject><subject>Macromolecular Substances - metabolism</subject><subject>Male</subject><subject>Molecular Sequence Data</subject><subject>Nerve Tissue Proteins - genetics</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Neurons, Afferent - metabolism</subject><subject>Nodose Ganglion - metabolism</subject><subject>Potassium Channels - genetics</subject><subject>Potassium Channels - metabolism</subject><subject>Potassium Channels, Voltage-Gated - metabolism</subject><subject>Protein Isoforms - genetics</subject><subject>Protein Isoforms - metabolism</subject><subject>Protein Subunits - metabolism</subject><subject>Rats</subject><subject>Rats, Sprague-Dawley</subject><subject>Sequence Homology, Amino Acid</subject><subject>Shal Potassium Channels</subject><issn>1044-7431</issn><issn>1095-9327</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1vFSEUhonR2A_9AW6aWbmbka-5QLoyjVpjEzd1TRg4WG4GmMLcVv-93N6bdGdXB8JzTg7vg9AHggeCyebTdog2DRTjccB0wJi9QqcEq7FXjIrX-zPnveCMnKCzWre4gVSxt-iEjIoQNo6naLotJtUIcWoVupBWKMauIacuggtmhdrZHJcZ_nQ-l2ieniZYHwFSt8CyBmcqdHc55jn_3jXcJNf9eOCdvTMpwVzfoTfezBXeH-s5-vX1y-3VdX_z89v3q883veVCrT0bnZdUbYyTwnsJDBMvJAdJOGFETYwqT61tNylHNlGrmNsI6YBYR70X7Bx9PMxdSr5vi6w6hmphntvH8q7qBm9GIeiLIMWSCNFyewkkgnEupGogOYC25FoLeL2UEE35qwnWe1V6q5sqvVelMdVNVeu5OA7fTS3q546jmwZcHoCWITwEKLraAMk2LQXsql0O_xn_D1DYpRc</recordid><startdate>20050601</startdate><enddate>20050601</enddate><creator>Ren, Xiaomeng</creator><creator>Hayashi, Yukio</creator><creator>Yoshimura, Naoki</creator><creator>Takimoto, Koichi</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TK</scope><scope>7X8</scope></search><sort><creationdate>20050601</creationdate><title>Transmembrane interaction mediates complex formation between peptidase homologues and Kv4 channels</title><author>Ren, Xiaomeng ; Hayashi, Yukio ; Yoshimura, Naoki ; Takimoto, Koichi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c479t-35df8296ad87ff8e301f784e8141319b329f2cc1418853b2c93d678de1cd2ff73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Alternative Splicing - physiology</topic><topic>Animals</topic><topic>Cell Membrane - metabolism</topic><topic>CHO Cells</topic><topic>Cricetinae</topic><topic>Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - genetics</topic><topic>Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - metabolism</topic><topic>Ganglia, Spinal - metabolism</topic><topic>Humans</topic><topic>Ion Channel Gating - physiology</topic><topic>Macromolecular Substances - metabolism</topic><topic>Male</topic><topic>Molecular Sequence Data</topic><topic>Nerve Tissue Proteins - genetics</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Neurons, Afferent - metabolism</topic><topic>Nodose Ganglion - metabolism</topic><topic>Potassium Channels - genetics</topic><topic>Potassium Channels - metabolism</topic><topic>Potassium Channels, Voltage-Gated - metabolism</topic><topic>Protein Isoforms - genetics</topic><topic>Protein Isoforms - metabolism</topic><topic>Protein Subunits - metabolism</topic><topic>Rats</topic><topic>Rats, Sprague-Dawley</topic><topic>Sequence Homology, Amino Acid</topic><topic>Shal Potassium Channels</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ren, Xiaomeng</creatorcontrib><creatorcontrib>Hayashi, Yukio</creatorcontrib><creatorcontrib>Yoshimura, Naoki</creatorcontrib><creatorcontrib>Takimoto, Koichi</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular and cellular neuroscience</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ren, Xiaomeng</au><au>Hayashi, Yukio</au><au>Yoshimura, Naoki</au><au>Takimoto, Koichi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Transmembrane interaction mediates complex formation between peptidase homologues and Kv4 channels</atitle><jtitle>Molecular and cellular neuroscience</jtitle><addtitle>Mol Cell Neurosci</addtitle><date>2005-06-01</date><risdate>2005</risdate><volume>29</volume><issue>2</issue><spage>320</spage><epage>332</epage><pages>320-332</pages><issn>1044-7431</issn><eissn>1095-9327</eissn><abstract>An asthma-related peptidase homologue (DPP10) may act as an auxiliary subunit of Kv4 channels, similar to DPPX. Here we show that DPP10 preferentially binds to Kv4 channel proteins to increase current density and alter channel gating. DPP10 also forms complexes by themselves and with DPPX in the absence of Kv4 channels. DPP10 mRNA is abundantly expressed in nodose and dorsal root ganglia, suggesting that DPP10 participates in controlling airway reactivity and mechanosensation. The region from the N-terminus to the end of the transmembrane of DPP10 mediates its association with the channel, whereas the S1–S2 portion of the channel is sufficient for complex formation. This N-terminal portion of DPP10 also confers all the gating effects produced by the peptidase homologue. Thus, interaction between transmembranes of DPP10/DPPX and Kv4 channel mediates functional complex formation. We call this protein DPPY, instead of DPP10, because of its revealed role as a Kv4 channel regulator.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>15911355</pmid><doi>10.1016/j.mcn.2005.02.003</doi><tpages>13</tpages></addata></record> |
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| subjects | Alternative Splicing - physiology Animals Cell Membrane - metabolism CHO Cells Cricetinae Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - genetics Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - metabolism Ganglia, Spinal - metabolism Humans Ion Channel Gating - physiology Macromolecular Substances - metabolism Male Molecular Sequence Data Nerve Tissue Proteins - genetics Nerve Tissue Proteins - metabolism Neurons, Afferent - metabolism Nodose Ganglion - metabolism Potassium Channels - genetics Potassium Channels - metabolism Potassium Channels, Voltage-Gated - metabolism Protein Isoforms - genetics Protein Isoforms - metabolism Protein Subunits - metabolism Rats Rats, Sprague-Dawley Sequence Homology, Amino Acid Shal Potassium Channels |
| title | Transmembrane interaction mediates complex formation between peptidase homologues and Kv4 channels |
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